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Information on EC 4.1.2.44 - 2,3-epoxybenzoyl-CoA dihydrolase and Organism(s) Aromatoleum evansii and UniProt Accession Q84HH6

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.44 2,3-epoxybenzoyl-CoA dihydrolase
IUBMB Comments
The enzyme is involved in the aerobic benzoyl-CoA catabolic pathway of the bacterium Azoarcus evansii. The enzyme converts 2,3-epoxy-2,3-dihydrobenzoyl-CoA to its oxepin form prior to the ring-opening and the formation of a dialdehyde intermediate.
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This record set is specific for:
Aromatoleum evansii
UNIPROT: Q84HH6
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The taxonomic range for the selected organisms is: Aromatoleum evansii
The enzyme appears in selected viruses and cellular organisms
Synonyms
benzoyl-coa-dihydrodiol lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,3-epoxybenzoyl-CoA dihydrolase
-
benzoyl-CoA oxidation component C
-
benzoyl-CoA-dihydrodiol lyase
formerly termed
dihydrodiol transforming enzyme
-
SYSTEMATIC NAME
IUBMB Comments
2,3-epoxy-2,3-dihydrobenzoyl-CoA (3Z)-6-oxohex-3-enoyl-CoA-lyase (formate-forming)
The enzyme is involved in the aerobic benzoyl-CoA catabolic pathway of the bacterium Azoarcus evansii. The enzyme converts 2,3-epoxy-2,3-dihydrobenzoyl-CoA to its oxepin form prior to the ring-opening and the formation of a dialdehyde intermediate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
3,4-dehydroadipyl-CoA semialdehyde + formate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-dihydro-2,3-dihydroxybenzoyl-CoA + H2O
3,4-dehydroadipyl-CoA semialdehyde + formate
show the reaction diagram
the enzyme is involved in the aerobic benzoyl-CoA catabolic pathway. Benzoyl-CoA is oxidized to 2,3-dihydro-2,3-dihydroxybenzoyl-CoA (benzoyl-CoA dihydrodiol) by benzoyl-CoA oxygenase/reductase BoxBA in the presence of molecular oxygen. The next, ring cleaving step is catalysed by BoxC
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
2,3-dihydro-2,3-dihydroxybenzoyl-CoA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
2,3-dihydro-2,3-dihydroxybenzoyl-CoA
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
half maximal activity at pH 7 and pH 11
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.44
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BOXC_AROEV
555
0
61083
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
gel filtration
60000
2 * 60000, SDS-PAGE
61000
x * 61000, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 61000, calculated from sequence
homodimer
2 * 60000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, the protein can be stored without appreciable loss of activity for months in the presence of 10% (v/v) glycerol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild type and recombinant proteins
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the boxC gene is expressed in a recombinant Escherichia coli strain as a fusion protein with maltose binding protein (BoxCmal)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gescher, J.; Zaar, A.; Mohamed, M.; Schgger, H.; Fuchs, G.
Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus evansii
J. Bacteriol.
184
6301-6315
2002
Aromatoleum evansii (Q84HH6)
Manually annotated by BRENDA team
Gescher, J.; Eisenreich, W.; Wrth, J.; Bacher, A.; Fuchs, G.
Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme
Mol. Microbiol.
56
1586-1600
2005
Aromatoleum evansii (Q84HH6), Aromatoleum evansii
Manually annotated by BRENDA team
Rather, L.J.; Knapp, B.; Haehnel, W.; Fuchs, G.
Coenzyme A-dependent aerobic metabolism of benzoate via epoxide formation
J. Biol. Chem.
285
20615-20624
2010
Aromatoleum evansii (Q84HH6), Aromatoleum evansii KB740 (DSM Z6869) (Q84HH6)
Manually annotated by BRENDA team